PMID: 375199Mar 1, 1979Paper

Chemical modification study of aminoacyl-tRNA conformation

Nucleic Acids Research
K NegishiH Hayatsu

Abstract

Chemical reactivity of cytosines in 32P-labeled E. coli tRNA1Leu, E. coli tRNAPhe and yeast tRNAPhe before and after aminoacylation was examined by use of a cytosine-specific reagent, semicarbazide-bisulfite mixture. In all the three tRNA species examined, the cytosine residues that were susceptible to the modification were the same in the aminoacylated tRNA and the unacylated tRNA. Only a limited number of the cytosine residues were modifiable: those that occur in the anticodon, the 3'-CCA terminus, the D-loop, and the extra loop. The sites accessible by the reagent are in good agreement with the general three-dimensional structure of tRNA proposed in literature. These results indicate that the gross conformation of these tRNAs does not change on aminoacylation, and consequently favor the view that the T psi C(G) sequence could become exposed in later steps of protein synthesis in order to achieve the binding of aminoacyl tRNA to ribosomes.

References

Jan 1, 1976·Annual Review of Biochemistry·A Rich, U L RajBhandary
Aug 23, 1976·Biochemical and Biophysical Research Communications·O PongsV A Erdmann
Dec 1, 1976·Nucleic Acids Research·M Lowdon, J P Goddard
Feb 5, 1973·Biochemical and Biophysical Research Communications·M Yoshida
Sep 18, 1973·Biochemical and Biophysical Research Communications·G J ThomasS C Mohr
Aug 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·Y P WongD R Kearns
Sep 1, 1963·Biochemistry·R WOLFENDEN

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